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Structural determinants of Cys 2 His 2 zinc fingers
Author(s) -
Mortishire-Smith Russell J.,
Lee Min S.,
Bolinger Lizann,
Wright Peter E.
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80392-t
Subject(s) - zinc , chemistry , crystallography , organic chemistry
Two mutants of the zinc finger peptide Xfin‐31 (Ac‐YKCGLCERSFVEKSALSRHQRVHKN‐CONH 2 ) containing alterations to the conserved hydrophobic core have been constructed and their zinc‐bound structures investigated by 1 H NMR techniques. In the first (Xfin‐31B) a double mutation R8F/F10G places the conserved core aromatic residue at position 8 rather than position 10. In the second (Xfin‐31C), Phe‐10 is replaced by Leu. A qualitative analysis of 1 H chemical shifts, NOE connectivities and coupling constants indicates that the global folds of both mutants are similar to that of the wild‐type protein. However, amide exchange rates suggest that the F10L mutant is much less stable than either the wild‐type or the R8F/F10G mutant.